ABR_HUMAN
ID ABR_HUMAN Reviewed; 859 AA.
AC Q12979; B3KW89; B7Z6H7; D3DTH3; D3DTH4; F5H3S2; F5H8B3; Q13693; Q13694;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Active breakpoint cluster region-related protein {ECO:0000305};
GN Name=ABR {ECO:0000312|HGNC:HGNC:81};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Hippocampus;
RX PubMed=8262969; DOI=10.1016/s0021-9258(19)74248-3;
RA Tan E.-C., Leung T., Manser E., Lim L.;
RT "The human active breakpoint cluster region-related gene encodes a brain
RT protein with homology to guanine nucleotide exchange proteins and GTPase-
RT activating proteins.";
RL J. Biol. Chem. 268:27291-27298(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP ARG-517.
RC TISSUE=Cerebellum, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Fibroblast;
RX PubMed=8349582; DOI=10.1016/s0021-9258(19)85281-x;
RA Heisterkamp N., Kaartinen V., van Soest S., Bokoch G.M., Groffen J.;
RT "Human ABR encodes a protein with GAPrac activity and homology to the DBL
RT nucleotide exchange factor domain.";
RL J. Biol. Chem. 268:16903-16906(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 436-597.
RX PubMed=2587217; DOI=10.1093/nar/17.21.8821;
RA Heisterkamp N., Morris C., Groffen J.;
RT "ABR, an active BCR-related gene.";
RL Nucleic Acids Res. 17:8821-8831(1989).
RN [7]
RP FUNCTION, AND DOMAIN.
RX PubMed=7479768; DOI=10.1073/pnas.92.22.10282;
RA Chuang T.H., Xu X., Kaartinen V., Heisterkamp N., Groffen J., Bokoch G.M.;
RT "Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10282-10286(1995).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-683 AND ASN-795.
RX PubMed=17116687; DOI=10.1128/mcb.00756-06;
RA Cho Y.J., Cunnick J.M., Yi S.J., Kaartinen V., Groffen J., Heisterkamp N.;
RT "Abr and Bcr, two homologous Rac GTPase-activating proteins, control
RT multiple cellular functions of murine macrophages.";
RL Mol. Cell. Biol. 27:899-911(2007).
RN [9]
RP FUNCTION, INTERACTION WITH DLG4, AND MUTAGENESIS OF VAL-859.
RX PubMed=20962234; DOI=10.1523/jneurosci.1711-10.2010;
RA Oh D., Han S., Seo J., Lee J.R., Choi J., Groffen J., Kim K., Cho Y.S.,
RA Choi H.S., Shin H., Woo J., Won H., Park S.K., Kim S.Y., Jo J.,
RA Whitcomb D.J., Cho K., Kim H., Bae Y.C., Heisterkamp N., Choi S.Y., Kim E.;
RT "Regulation of synaptic Rac1 activity, long-term potentiation maintenance,
RT and learning and memory by BCR and ABR Rac GTPase-activating proteins.";
RL J. Neurosci. 30:14134-14144(2010).
CC -!- FUNCTION: Protein with a unique structure having two opposing
CC regulatory activities toward small GTP-binding proteins. The C-terminus
CC is a GTPase-activating protein domain which stimulates GTP hydrolysis
CC by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP
CC hydrolysis of RAC1 or CDC42, leading to down-regulation of the active
CC GTP-bound form (PubMed:7479768, PubMed:17116687). The central Dbl
CC homology (DH) domain functions as guanine nucleotide exchange factor
CC (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the
CC conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound
CC form (PubMed:7479768). Functions as an important negative regulator of
CC neuronal RAC1 activity (By similarity). Regulates macrophage functions
CC such as CSF-1 directed motility and phagocytosis through the modulation
CC of RAC1 activity (By similarity). {ECO:0000250|UniProtKB:Q5SSL4,
CC ECO:0000269|PubMed:17116687, ECO:0000269|PubMed:7479768}.
CC -!- SUBUNIT: Interacts with DLG4. {ECO:0000269|PubMed:20962234}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q5SSL4}. Synapse
CC {ECO:0000250|UniProtKB:A0A0G2JTR4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Long;
CC IsoId=Q12979-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q12979-2; Sequence=VSP_001815;
CC Name=3;
CC IsoId=Q12979-3; Sequence=VSP_046029, VSP_046030;
CC Name=4;
CC IsoId=Q12979-4; Sequence=VSP_046148;
CC -!- TISSUE SPECIFICITY: Highly enriched in the brain. Much weaker
CC expression in heart, lung and muscle.
CC -!- DOMAIN: The central Dbl homology (DH) domain functions as guanine
CC nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA
CC and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-
CC bound to the GTP-bound form. The C-terminus is a Rho-GAP domain which
CC stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a
CC unique structure having two opposing regulatory activities toward small
CC GTP-binding proteins. {ECO:0000305|PubMed:7479768}.
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DR EMBL; U01147; AAC50063.1; -; mRNA.
DR EMBL; L19704; AAC37519.1; -; Genomic_DNA.
DR EMBL; L19705; AAC37518.1; -; Genomic_DNA.
DR EMBL; AK124547; BAG54051.1; -; mRNA.
DR EMBL; AK300336; BAH13263.1; -; mRNA.
DR EMBL; AC015884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90631.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90633.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90634.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90635.1; -; Genomic_DNA.
DR CCDS; CCDS10999.1; -. [Q12979-1]
DR CCDS; CCDS11000.1; -. [Q12979-2]
DR CCDS; CCDS54060.1; -. [Q12979-4]
DR CCDS; CCDS58497.1; -. [Q12979-3]
DR PIR; A47485; A47485.
DR PIR; A49307; A49307.
DR RefSeq; NP_001083.2; NM_001092.4. [Q12979-2]
DR RefSeq; NP_001153218.1; NM_001159746.2. [Q12979-4]
DR RefSeq; NP_001243776.1; NM_001256847.2. [Q12979-3]
DR RefSeq; NP_001269078.1; NM_001282149.1.
DR RefSeq; NP_001309769.1; NM_001322840.1. [Q12979-4]
DR RefSeq; NP_068781.2; NM_021962.4. [Q12979-1]
DR AlphaFoldDB; Q12979; -.
DR SMR; Q12979; -.
DR BioGRID; 106547; 32.
DR IntAct; Q12979; 8.
DR MINT; Q12979; -.
DR STRING; 9606.ENSP00000303909; -.
DR iPTMnet; Q12979; -.
DR PhosphoSitePlus; Q12979; -.
DR BioMuta; ABR; -.
DR DMDM; 357528764; -.
DR EPD; Q12979; -.
DR jPOST; Q12979; -.
DR MassIVE; Q12979; -.
DR MaxQB; Q12979; -.
DR PaxDb; Q12979; -.
DR PeptideAtlas; Q12979; -.
DR PRIDE; Q12979; -.
DR ProteomicsDB; 26359; -.
DR ProteomicsDB; 27736; -.
DR ProteomicsDB; 59072; -. [Q12979-1]
DR ProteomicsDB; 59073; -. [Q12979-2]
DR Antibodypedia; 22668; 74 antibodies from 18 providers.
DR DNASU; 29; -.
DR Ensembl; ENST00000291107.6; ENSP00000291107.2; ENSG00000159842.16. [Q12979-2]
DR Ensembl; ENST00000302538.10; ENSP00000303909.5; ENSG00000159842.16. [Q12979-1]
DR Ensembl; ENST00000543210.6; ENSP00000445198.2; ENSG00000159842.16. [Q12979-3]
DR Ensembl; ENST00000544583.6; ENSP00000442048.2; ENSG00000159842.16. [Q12979-4]
DR Ensembl; ENST00000611009.4; ENSP00000484030.1; ENSG00000276016.4. [Q12979-3]
DR Ensembl; ENST00000611021.3; ENSP00000483168.1; ENSG00000278741.4. [Q12979-2]
DR Ensembl; ENST00000612118.4; ENSP00000481740.1; ENSG00000278741.4. [Q12979-1]
DR Ensembl; ENST00000615642.4; ENSP00000479455.1; ENSG00000278741.4. [Q12979-3]
DR Ensembl; ENST00000620619.4; ENSP00000478880.1; ENSG00000278741.4. [Q12979-4]
DR Ensembl; ENST00000625740.2; ENSP00000486511.1; ENSG00000276016.4. [Q12979-2]
DR Ensembl; ENST00000627258.2; ENSP00000486214.1; ENSG00000278741.4. [Q12979-4]
DR GeneID; 29; -.
DR KEGG; hsa:29; -.
DR MANE-Select; ENST00000302538.10; ENSP00000303909.5; NM_021962.5; NP_068781.2.
DR UCSC; uc002fsd.6; human. [Q12979-1]
DR CTD; 29; -.
DR DisGeNET; 29; -.
DR GeneCards; ABR; -.
DR HGNC; HGNC:81; ABR.
DR HPA; ENSG00000159842; Low tissue specificity.
DR MIM; 600365; gene.
DR neXtProt; NX_Q12979; -.
DR OpenTargets; ENSG00000159842; -.
DR PharmGKB; PA24417; -.
DR VEuPathDB; HostDB:ENSG00000159842; -.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00940000153491; -.
DR HOGENOM; CLU_004000_1_0_1; -.
DR InParanoid; Q12979; -.
DR OMA; RILCYEN; -.
DR OrthoDB; 762492at2759; -.
DR PhylomeDB; Q12979; -.
DR TreeFam; TF105082; -.
DR PathwayCommons; Q12979; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q12979; -.
DR SIGNOR; Q12979; -.
DR BioGRID-ORCS; 29; 16 hits in 1067 CRISPR screens.
DR ChiTaRS; ABR; human.
DR GenomeRNAi; 29; -.
DR Pharos; Q12979; Tbio.
DR PRO; PR:Q12979; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q12979; protein.
DR Bgee; ENSG00000159842; Expressed in superior frontal gyrus and 100 other tissues.
DR ExpressionAtlas; Q12979; baseline and differential.
DR Genevisible; Q12979; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR CDD; cd13366; PH_ABR; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR037865; ABR_PH.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23182; PTHR23182; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; GTPase activation;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..859
FT /note="Active breakpoint cluster region-related protein"
FT /id="PRO_0000080902"
FT DOMAIN 91..284
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 301..459
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 484..613
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 647..845
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 26..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSL4"
FT VAR_SEQ 1..82
FT /note="MEPLSHRGLPRLSWIDTLYSNFSYGTDEYDGEGNEEQKGPPEGSETMPYIDE
FT SPTMSPQLSARSQGGGDGVSPTPPEGLAPG -> MEEEEEAIGLLDKVLEDEDVFLLEE
FT CELGTPTSPGSGSPFLVAVK (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001815"
FT VAR_SEQ 1..48
FT /note="MEPLSHRGLPRLSWIDTLYSNFSYGTDEYDGEGNEEQKGPPEGSETMP ->
FT MTDVLPQPDCSPKAGREPLALEESGSKRPPNTGARLWGRVRNKLLRNK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046029"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046148"
FT VAR_SEQ 49..597
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046030"
FT VARIANT 517
FT /note="K -> R (in dbSNP:rs34169260)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057186"
FT MUTAGEN 683
FT /note="R->A: Reduces GAP activity. Loss of GAP activity;
FT when associated with A-795."
FT /evidence="ECO:0000269|PubMed:17116687"
FT MUTAGEN 795
FT /note="N->A: Loss of GAP activity; when associated with A-
FT 683."
FT /evidence="ECO:0000269|PubMed:17116687"
FT MUTAGEN 859
FT /note="V->A: Abolishes interaction with DLG4. No effect on
FT synaptic localization."
FT /evidence="ECO:0000269|PubMed:20962234"
FT CONFLICT 67
FT /note="G -> R (in Ref. 1; AAC50063)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="R -> K (in Ref. 2; BAG54051)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="K -> R (in Ref. 2; BAH13263)"
FT /evidence="ECO:0000305"
FT CONFLICT 657..660
FT /note="RSKV -> VQGA (in Ref. 3; AAC37519)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="L -> V (in Ref. 3; AAC37519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 97598 MW; 3A5BE3AD2455A194 CRC64;
MEPLSHRGLP RLSWIDTLYS NFSYGTDEYD GEGNEEQKGP PEGSETMPYI DESPTMSPQL
SARSQGGGDG VSPTPPEGLA PGVEAGKGLE MRKLVLSGFL ASEEIYINQL EALLLPMKPL
KATATTSQPV LTIQQIETIF YKIQDIYEIH KEFYDNLCPK VQQWDSQVTM GHLFQKLASQ
LGVYKAFVDN YKVALETAEK CSQSNNQFQK ISEELKVKGP KDSKDSHTSV TMEALLYKPI
DRVTRSTLVL HDLLKHTPVD HPDYPLLQDA LRISQNFLSS INEDIDPRRT AVTTPKGETR
QLVKDGFLVE VSESSRKLRH VFLFTDVLLC AKLKKTSAGK HQQYDCKWYI PLADLVFPSP
EESEASPQVH PFPDHELEDM KMKISALKSE IQKEKANKGQ SRAIERLKKK MFENEFLLLL
NSPTIPFRIH NRNGKSYLFL LSSDYERSEW REAIQKLQKK DLQAFVLSSV ELQVLTGSCF
KLRTVHNIPV TSNKDDDESP GLYGFLHVIV HSAKGFKQSA NLYCTLEVDS FGYFVSKAKT
RVFRDTAEPK WDEEFEIELE GSQSLRILCY EKCYDKTKVN KDNNEIVDKI MGKGQIQLDP
QTVETKNWHT DVIEMNGIKV EFSMKFTSRD MSLKRTPSKK QTGVFGVKIS VVTKRERSKV
PYIVRQCVEE VEKRGIEEVG IYRISGVATD IQALKAVFDA NNKDILLMLS DMDINAIAGT
LKLYFRELPE PLLTDRLYPA FMEGIALSDP AAKENCMMHL LRSLPDPNLI TFLFLLEHLK
RVAEKEPINK MSLHNLATVF GPTLLRPSEV ESKAHLTSAA DIWSHDVMAQ VQVLLYYLQH
PPISFAELKR NTLYFSTDV
